MASE1 and MASE2: two novel integral membrane sensory domains

J Mol Microbiol Biotechnol. 2003;5(1):11-6. doi: 10.1159/000068720.

Abstract

Escherichia coli proteins YegE and YaiC contain N-terminal integral membrane regions, followed by the putative diguanylate cyclase (GGDEF, DUF1) domains. The membrane domains of these proteins, named MASE1 (membrane-associated sensor) and MASE2, respectively, were found in other bacterial signaling proteins, such as histidine kinases (MASE1) and an adenylate cyclase (MASE2). Although the nature of the signals sensed by MASE1 and MASE2 is still unknown, MASE1-containing receptors appear to play important roles in bacteria, including iron and/or oxygen sensing by hemerythrine-containing proteins in the sulfate-reducing bacterium Desulfovibrio vulgaris.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenylyl Cyclases / chemistry*
  • Adenylyl Cyclases / genetics
  • Amino Acid Sequence
  • Escherichia coli / chemistry
  • Escherichia coli / enzymology*
  • Histidine Kinase
  • Molecular Sequence Data
  • Protein Kinases / chemistry*
  • Protein Kinases / genetics
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Signal Transduction*

Substances

  • Protein Kinases
  • Histidine Kinase
  • Adenylyl Cyclases